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Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase genes of tomato (Solanum lycopersicum L.) and analysis of their differential expression in response to temperature
- In plants, the trehalose biosynthetic pathway plays key roles in the regulation of carbon allocation and stress adaptation.
Engineering of the pathway holds great promise to increase the stress resilience of crop plants.
The synthesis of trehalose proceeds by a two-step pathway in which a trehalose-phosphate synthase (TPS) uses UDP-glucose and glucose-6-phosphate to produce trehalose-6 phosphate (T6P) that is subsequently dephosphorylated by trehalose-6 phosphate phosphatase (TPP).
While plants usually do not accumulate high amounts of trehalose, their genome encodes large families of putative trehalose biosynthesis genes, with many members lacking obvious enzymatic activity.
Thus, the function of putative trehalose biosynthetic proteins in plants is only vaguely understood. To gain a deeper insight into the role of trehalose biosynthetic proteins in crops, we assessed the enzymatic activity of the TPS/TPP family from tomato (Solanum lycopersicum L.) and investigated their expression pattern in different tissues as well as inIn plants, the trehalose biosynthetic pathway plays key roles in the regulation of carbon allocation and stress adaptation.
Engineering of the pathway holds great promise to increase the stress resilience of crop plants.
The synthesis of trehalose proceeds by a two-step pathway in which a trehalose-phosphate synthase (TPS) uses UDP-glucose and glucose-6-phosphate to produce trehalose-6 phosphate (T6P) that is subsequently dephosphorylated by trehalose-6 phosphate phosphatase (TPP).
While plants usually do not accumulate high amounts of trehalose, their genome encodes large families of putative trehalose biosynthesis genes, with many members lacking obvious enzymatic activity.
Thus, the function of putative trehalose biosynthetic proteins in plants is only vaguely understood. To gain a deeper insight into the role of trehalose biosynthetic proteins in crops, we assessed the enzymatic activity of the TPS/TPP family from tomato (Solanum lycopersicum L.) and investigated their expression pattern in different tissues as well as in response to temperature shifts. From the 10 TPS isoforms tested, only the 2 proteins belonging to class I showed enzymatic activity, while all 5 TPP isoforms investigated were catalytically active.
Most of the TPS/TPP family members showed the highest expression in mature leaves, and promoter-reporter gene studies suggest that the two class I TPS genes have largely overlapping expression patterns within the vasculature, with only subtle differences in expression in fruits and flowers.
The majority of tomato TPS/TPP genes were induced by heat stress, and individual family members also responded to cold.
This suggests that trehalose biosynthetic pathway genes could play an important role during temperature stress adaptation.
In summary, our study represents a further step toward the exploitation of the TPS and TPP gene families for the improvement of tomato stress resistance.…
Author details: | Mohanna Mollavali, Frederik BörnkeORCiDGND |
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DOI: | https://doi.org/10.3390/ijms231911436 |
ISSN: | 1661-6596 |
ISSN: | 1422-0067 |
Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/36232739 |
Title of parent work (English): | International journal of molecular sciences |
Publisher: | MDPI |
Place of publishing: | Basel |
Publication type: | Article |
Language: | English |
Date of first publication: | 2022/09/28 |
Publication year: | 2022 |
Release date: | 2024/08/12 |
Tag: | Solanum lycopersicum; heat stress; trehalose metabolism; yeast complementation |
Volume: | 23 |
Issue: | 19 |
Article number: | 11436 |
Number of pages: | 17 |
Funding institution: | Bundesministerium fur Ernahrung und Landwirtschaft [2816DOKI08]; Federal; Republic of Germany |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
DDC classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Peer review: | Referiert |
Publishing method: | Open Access / Gold Open-Access |
DOAJ gelistet | |
License (German): | ![]() |